Peptide synthesis by means of immobilized enzymes |
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Authors: | Andreas Könnecke Ralf Bullerjahn Hans-Dieter Jakubke |
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Institution: | (1) Sektion Biowissenschaften, Bereich Biochemie, Karl-Marx-Universität, DDR-701 Leipzig, German Democratic Republic |
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Abstract: | -Chymotrypsin covalently bound to silica, enzacryl AA, and enzacryl AH catalyzes peptide bond formation between N-protected dipeptide methyl esters and H-Leu-NH2 with results similar to those with the free enzyme. The influence of water-miscible and water-immiscible cosolvents, of the supports, and of the structure of the substrates is shown to be of importance for the ease of the chymotrypsin-medicated coupling reactions. The best yields were obtained using biphasic aqueous-organic solvent mixtures, silica-bound chymotrypsin, and substrates with leucine in the P2-position. The yields of the syntheses are discussed in terms of the reactivity of substrates with similar structure in enzymatic hydrolyses. All the immobilized chymotrypsin preparations could be re-utilized successfully for further couplings.
Abbreviations: IUPAC/IUB rules for peptides are followed, see Eur. J. Biochem.27, 201 (1972); Glt=4-carboxybutyrul (glutaryl),-Nan=4-nitroanilide. All amino acids except glycine are of L-configuration. |
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Keywords: | Biphasic aqueous-organic solvent mixtures -Chymotrypsin" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">-Chymotrypsin Immobilized enzymes Peptide synthesis |
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